Glycosylation of bacterial cellulases prevents proteolytic cleavage between functional domains.

Abstract:

:Glycosylated cellulases from Cellulomonas fimi were compared with their non-glycosylated counterparts synthesized in Escherichia coli from recombinant DNA. Glycosylation of the enzymes does not significantly affect their kinetic properties, or their stabilities towards heat and pH. However, the glycosylated enzymes are protected from attack by a C. fimi protease when bound to cellulose, while the non-glycosylated enzymes yield active, truncated products with greatly reduced affinity for cellulose.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Langsford ML,Gilkes NR,Singh B,Moser B,Miller RC Jr,Warren RA,Kilburn DG

doi

10.1016/0014-5793(87)81150-x

subject

Has Abstract

pub_date

1987-12-10 00:00:00

pages

163-7

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)81150-X

journal_volume

225

pub_type

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